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The articular cartilage function is dependent on the molecular composition of the extracellular matrix (ECM). The ECM consists mainly of proteoglycan and collagens . The main proteoglycan in cartilage is aggrecan, which, as its name suggests, forms large aggregates with hyaluronan and with itself. [ 8 ]
The chondrocyte in cartilage matrix has rounded or polygonal structure. The exception occurs at tissue boundaries, for example the articular surfaces of joints, in which chondrocytes may be flattened or discoid. Intra-cellular features are characteristic of a synthetically active cell.
12845 Ensembl ENSG00000105664 ENSMUSG00000031849 UniProt P49747 Q9R0G6 RefSeq (mRNA) NM_000095 NM_016685 RefSeq (protein) NP_000086 NP_057894 Location (UCSC) Chr 19: 18.78 – 18.79 Mb Chr 8: 70.83 – 70.83 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Cartilage oligomeric matrix protein (COMP), also known as thrombospondin-5, is an extracellular matrix (ECM) protein primarily ...
Collagen Type II fibers are responsible for giving the future cartilage matrix its tensile strength. The structure of these fibers, like the majority of collagen fibers, forms a triple helix structure. [3] Proteoglycans resist the compression generally put upon cartilage and generate the swelling pressure responsible for stress shielding the ...
In biology, matrix (pl.: matrices) is the material (or tissue) in between a eukaryotic organism's cells. The structure of connective tissues is an extracellular matrix. Fingernails and toenails grow from matrices. It is found in various connective tissues. It serves as a jelly-like structure instead of cytoplasm in connective tissue.
Aggrecan is a critical component for cartilage structure and the function of joints. Functionally, the G1 domain interacts with hyaluronic acid and link protein, forming stable ternary complexes in the extracellular matrix. G2 is homologous to the tandem repeats of G1 and of link protein and is involved in product processing.
The collagen protein is composed of a triple helix, which generally consists of two identical chains (α1) and an additional chain that differs slightly in its chemical composition (α2). [23] The amino acid composition of collagen is atypical for proteins, particularly with respect to its high hydroxyproline content.
Type II collagen is the basis for hyaline cartilage, including the articular cartilages at joint surfaces. It is formed by homotrimers of collagen, type II, alpha 1 chains. It makes up 50% of all protein in cartilage and 85–90% of collagen of articular cartilage. Type II collagen is organised into fibrils.